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Associate Professor Lynette Cegelski's research is inspired by the challenge and importance of elucidating chemical structure and function in biological systems and the need for new and unconventional strategies to treat infectious diseases. Cegelski completed her undergraduate studies in Chemistry at SUNY-Binghamton, New York (B.S. summa cum laude and Phi Beta Kappa 1998), where she participated in research to determine the microtubule-bound conformation of the anti-cancer drug Taxol by REDOR solid-state NMR. This formative experience motivated her move to Washington University to conduct her PhD training in the laboratory of Professor Jacob Schaefer (Ph.D. Chemistry 2004). She investigated bacterial and plant macromolecular and whole-cell systems using solid-state NMR, including examining the mode of action of the antibiotic oritavancin and investigating photosynthesis and photorespiration in soybean leaves with 13CO2 and 15N labeling. She introduced the use of 4-frequency TEDOR-REDOR measurements in whole cells for the first time. She trained in Microbiology and Infectious Disease research as a postdoctoral fellow in Molecular Microbiology at the Washington University School of Medicine, working with Professor Scott Hultgren. There, she defined amyloid contributions to E. coli biofilms and introduced the first small-molecule inhibitors of functional amyloid assembly in bacteria. She joined the faculty of the Stanford Chemistry Department in 2008. The Cegelski Research program integrates chemistry, biology, and physics to investigate the assembly and function of macromolecular and whole-cell systems. They are revealing new bacterial structures, uncovering fundamental parameters of chemical composition and architecture in complex biofilm assemblies, and identifying new anti-infectives and anti-infective strategies. Cegelski's work has garnered early career awards, including the Burroughs Wellcome Career Award at the Scientific Interface, the 2010 NIH Director’s New Innovator Award, the National Science Foundation CAREER Award, and the Presidential Early Career Award for Scientists and Engineers (PECASE).
Our research program is inspired by the challenge and importance of elucidating chemical structure and function in complex biological systems and the need for new strategies to treat infectious diseases. The genomics and proteomics revolutions have been enormously successful in generating crucial "parts lists" for biological systems. Yet, for many fascinating systems, formidable challenges exist in building complete descriptions of how the parts function and assemble into macromolecular complexes and whole-cell factories. We have introduced uniquely enabling problem-solving approaches integrating solid-state NMR spectroscopy with microscopy and biochemical and biophysical tools to determine atomic- and molecular-level detail in complex macromolecular assemblies and whole cells and biofilms. We are uncovering new chemistry and new chemical structures produced in nature. We identify small molecules that influence bacterial assembly processes and use these in chemical genetics approaches to learn about bacterial cell wall, amyloid and biofilm assembly.Translationally, we have launched a collaborative antibacterial drug design program integrating synthesis, chemical biology, and mechanistic biochemistry and biophysics directed at the discovery and development of new antibacterial therapeutics targeting difficult-to-treat bacteria.